Purification of bovine serum paraoxonase and its immobilization on Eupergit C 250 L by covalent attachment.


Sayin M., Guler Ö.

Journal of enzyme inhibition and medicinal chemistry, cilt.30, ss.69-74, 2015 (SCI Expanded İndekslerine Giren Dergi) identifier identifier

  • Cilt numarası: 30 Konu: 1
  • Basım Tarihi: 2015
  • Doi Numarası: 10.3109/14756366.2013.879578
  • Dergi Adı: Journal of enzyme inhibition and medicinal chemistry
  • Sayfa Sayıları: ss.69-74

Özet

Serum paraoxonase (PON1) is a high-density lipoprotein (HDL)-associated enzyme that protects lipoproteins, both low-density lipoprotein (LDL) and HDL, against oxidation, and is considered as an antioxidative/anti-inflammatory component of HDL. In this study, PON1 was purified from bovine serum by ammonium sulfate precipitation and hydrophobic interaction chromatography on sepharose-4B-L-tyrosine-1-napthylamine. It was then immobilized on an unmodified Eupergit (R) C 250 L support. The immobilized PON1 retained a high catalytic activity and showed increased thermal stability compared to the native enzyme.